MAX Protein, Human (sf9, His-GST)

MAX, a transcription regulator, forms a sequence-specific DNA-binding protein complex either with MYC, promoting transcriptional activation, or with MAD, leading to transcriptional repression, recognizing the core sequence 5'-CAC[GA]TG-3'. MAX may act as a transcriptional repressor by recruiting a chromatin remodeling complex with H3 'Lys-9' histone methyltransferase activity and repressing MYC transcriptional activity from E-box elements. Efficient DNA binding requires dimerization with another bHLH protein. It binds DNA as a heterodimer with either MYC or MAD. MAX is part of the E2F6.com-1 complex during the G0 phase, along with various other components. It is also a component of some MLL1/MLL complexes, contributing to the regulation of gene expression. MAX interacts with SPAG9, and when in a heterodimer with MYC, it interacts with ABI1, potentially enhancing MYC:MAX transcriptional activity. MAX's versatility in forming complexes with different partners underscores its role as a key modulator of gene expression.